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Conserved domains on  [gi|537239411|gb|ERE86769|]
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Poly(ADP-ribose) polymerase, catalytic domain containing protein [Cricetulus griseus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF3827 super family cl28786
Domain of unknown function (DUF3827); This family contains the Swiss:Q9HCM3 protein which has ...
2188-2801 0e+00

Domain of unknown function (DUF3827); This family contains the Swiss:Q9HCM3 protein which has been found to be fused fused to BRAF gene in many cases of pilocytic astrocytomas. The fusion is due mainly to a tandem duplication of 2 Mb at 7q34. Although nothing is known about the function of Swiss:Q9HCM3 protein, the BRAF protein is a well characterized oncoprotein. It is a serine/threonine protein kinase which is implicated in MAP/ERK signalling, a critical pathway for the regulation of cell division, differentiation and secretion.


The actual alignment was detected with superfamily member pfam12877:

Pssm-ID: 463737  Cd Length: 677  Bit Score: 857.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2188 VPEPRFQVQTVLQFVPPSVDTGFCNFTQSVEKGLMTALFEV-RKHQGVYNLTVQIVNVTIGSSRVTPRRGPVNIIFAVKG 2266
Cdd:pfam12877    4 VPDYKFQVHTVLQFVPQHVDVRFCNFSQRIEKGLQMAFAEVeRRSLETTNFTVQILNITNALPEAQAQSQPVDITFAVRD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2267 THGFLNGSEVSDLLRNLTVVEFSFYLGYPVLQIAEPFQYPQLNLSQLLKSSWVRTVLLGVVERQLHNEVFPAEMERKLAQ 2346
Cdd:pfam12877   84 SRGYLNGSVVSNLLRQLSAVEFSFYLGFPVLQIAEPFHYPELNTSQLLRSSWVRTVLLGVDDQRVNERSFQALMERRLAL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2347 LLSEVPTRRRMWRRATvSAGNSVVQVVNVSRLEGDDNPVQLIYFVENQDGERLSAAQSSDLINKVDLQRAAIILGYRIQG 2426
Cdd:pfam12877  164 LLGESLGQGRRFKRAT-TVGNYSVQIVRVSRLPGPDNPAELTYFVEGPNGERLPATAAAKILNTVDVQRAAIILGYRVQG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2427 TIAQPVDRVKRPSPESQSGNLWVVVGVVIPVLVVTVIVVILYWKLCRTDKLDFQPDTVANIQQRQKLQIPSVKGFDFAKQ 2506
Cdd:pfam12877  243 VLAQPVEKVKNPPSETQPNNLWIIVGVVVPIAVVVIIIIILYWKLCRTDKLEFQPDTMSNIQQRQKLQAPSVKGFDFAKQ 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2507 HLGQHNKDDILIIHEPAPLPGPVKDhTTPSENGDVPSPKSKV---PSKNIRHRGRVSPSDADSTVSEESSERDAGDKAP- 2582
Cdd:pfam12877  323 HLGQHSKDDVPVIQEPAPLPLPVKD-ATPSENGEVPTPKSKTsskTSRGERRRGRISPSDGDSVGSDESSKRESGEESPr 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2583 --ATAHESKAHR------APQSGL-----SLSFFPVLTVV----------------------MARP-------------- 2613
Cdd:pfam12877  402 paATPSDGKQHRktnrpgNPMNGVseqlsSASIFEHVDRMsrgsadafrrssnkvqliamqpMPAPplhspplsdrsqes 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2614 ---KTKIQSALRHKSEIEHHRNKIRLRAKRRGHYEFPVVDDLSS--GDTKERHRVYRRAQMQIDKILDPAASVPSVFIEP 2688
Cdd:pfam12877  482 akiNKEIQKALRHKSEIEHHRNKIRLRAKRKGHYDFPAMDDIMKalTDRKEQRRIYQKAQKQIDKILDPDAHVPSPFTEP 561
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2689 RKSSRIKRSPKPRRKHQVNGCPADAEKDRLITTDSDGTYKRPPGVHNSAYIgcpSDPDLPADVQTPSSAELSRY------ 2762
Cdd:pfam12877  562 KKSSRGRRSPKQRRRQQNNGSPGDTEKDRLITRDSDGTYRKRPGVNNVAYV---SDPDQIPETNSPSPTDEVFYgpgsqp 638
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 537239411  2763 PGLPFSASQYIPPQPSIEEARQTMHSLLDDAFALVAPSS 2801
Cdd:pfam12877  639 KGHAPPPPPYLPPQPSIEEARQQMHSLLDDAFALVSPGS 677
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
868-977 6.23e-39

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


:

Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 142.07  E-value: 6.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  868 LLFHATCRVHVDYICRNNFDWIINDSRETKYGKGNYFAKEAMYSHKNC---SYEAKNIVMLVARVLAGNSIEGNMRYSSA 944
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 537239411  945 PA--------LYDSCVDSRLNPSVFVIFQKEQIYPAYVIEY 977
Cdd:cd01439    81 PLkpsgveldRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
5-66 2.93e-32

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


:

Pssm-ID: 465819  Cd Length: 62  Bit Score: 120.97  E-value: 2.93e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537239411     5 GVCCFITKILCAHGGRMTLEELLAEIALPEAQLRELLEAAGPDRFVQLEIVGQTGVTRSVVA 66
Cdd:pfam18606    1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
143-170 7.83e-15

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


:

Pssm-ID: 436636  Cd Length: 28  Bit Score: 70.19  E-value: 7.83e-15
                           10        20
                   ....*....|....*....|....*...
gi 537239411   143 PFFMPEICKSYKGEGRKQICGQPQPCER 170
Cdd:pfam18633    1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
1776-2092 3.16e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 59.20  E-value: 3.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1776 DFSAPAPSRSdvlALPSLTSSDPSTFLSQLFPTMTETFSLSNSidlQSPQLFVLNPTSLEPSQPWSSSDLLMKTVTLLPS 1855
Cdd:pfam17823   96 DLSEPATREG---AADGAASRALAAAASSSPSSAAQSLPAAIA---ALPSEAFSAPRAAACRANASAAPRAAIAAASAPH 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1856 HSemSPLPSSPLDSlkldeawrvsliesdvhlTSAFSDTTCVFDFSLIPHDSSVSTLVP----SSSETSLGISTAGTPLS 1931
Cdd:pfam17823  170 AA--SPAPRTAASS------------------TTAASSTTAASSAPTTAASSAPATLTPargiSTAATATGHPAAGTALA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1932 SLPTVS-----------HLTP--ILTESSPFSTLTPSDSSVSMTD---------HHTPVSLMSSSVIPTS---TESVSDL 1986
Cdd:pfam17823  230 AVGNSSpaagtvtaavgTVTPaaLATLAAAAGTVASAAGTINMGDpharrlspaKHMPSDTMARNPAAPMgaqAQGPIIQ 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1987 YLSASPTLASEVSPSPMPTRPVMGSSLIPTDLPPSTSPEPSSSPEPSMPDISTAPGDTVDSALNSEPMSQNPQGNSVPPP 2066
Cdd:pfam17823  310 VSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPT 389
                          330       340
                   ....*....|....*....|....*...
gi 537239411  2067 QPSLGPEITSTLE--ATVGTPALATAKP 2092
Cdd:pfam17823  390 QGAAGPGILLAPEqvATEATAGTASAGP 417
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
689-757 3.33e-07

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


:

Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 49.60  E-value: 3.33e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411   689 LWYWKDEFNKYVQYGDENkshlssnisSSYLESFFQS-CPRGVLPFQAGSQNYELSFQGMIQTNIASKTQ 757
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEV---------SSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTT 61
 
Name Accession Description Interval E-value
DUF3827 pfam12877
Domain of unknown function (DUF3827); This family contains the Swiss:Q9HCM3 protein which has ...
2188-2801 0e+00

Domain of unknown function (DUF3827); This family contains the Swiss:Q9HCM3 protein which has been found to be fused fused to BRAF gene in many cases of pilocytic astrocytomas. The fusion is due mainly to a tandem duplication of 2 Mb at 7q34. Although nothing is known about the function of Swiss:Q9HCM3 protein, the BRAF protein is a well characterized oncoprotein. It is a serine/threonine protein kinase which is implicated in MAP/ERK signalling, a critical pathway for the regulation of cell division, differentiation and secretion.


Pssm-ID: 463737  Cd Length: 677  Bit Score: 857.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2188 VPEPRFQVQTVLQFVPPSVDTGFCNFTQSVEKGLMTALFEV-RKHQGVYNLTVQIVNVTIGSSRVTPRRGPVNIIFAVKG 2266
Cdd:pfam12877    4 VPDYKFQVHTVLQFVPQHVDVRFCNFSQRIEKGLQMAFAEVeRRSLETTNFTVQILNITNALPEAQAQSQPVDITFAVRD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2267 THGFLNGSEVSDLLRNLTVVEFSFYLGYPVLQIAEPFQYPQLNLSQLLKSSWVRTVLLGVVERQLHNEVFPAEMERKLAQ 2346
Cdd:pfam12877   84 SRGYLNGSVVSNLLRQLSAVEFSFYLGFPVLQIAEPFHYPELNTSQLLRSSWVRTVLLGVDDQRVNERSFQALMERRLAL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2347 LLSEVPTRRRMWRRATvSAGNSVVQVVNVSRLEGDDNPVQLIYFVENQDGERLSAAQSSDLINKVDLQRAAIILGYRIQG 2426
Cdd:pfam12877  164 LLGESLGQGRRFKRAT-TVGNYSVQIVRVSRLPGPDNPAELTYFVEGPNGERLPATAAAKILNTVDVQRAAIILGYRVQG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2427 TIAQPVDRVKRPSPESQSGNLWVVVGVVIPVLVVTVIVVILYWKLCRTDKLDFQPDTVANIQQRQKLQIPSVKGFDFAKQ 2506
Cdd:pfam12877  243 VLAQPVEKVKNPPSETQPNNLWIIVGVVVPIAVVVIIIIILYWKLCRTDKLEFQPDTMSNIQQRQKLQAPSVKGFDFAKQ 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2507 HLGQHNKDDILIIHEPAPLPGPVKDhTTPSENGDVPSPKSKV---PSKNIRHRGRVSPSDADSTVSEESSERDAGDKAP- 2582
Cdd:pfam12877  323 HLGQHSKDDVPVIQEPAPLPLPVKD-ATPSENGEVPTPKSKTsskTSRGERRRGRISPSDGDSVGSDESSKRESGEESPr 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2583 --ATAHESKAHR------APQSGL-----SLSFFPVLTVV----------------------MARP-------------- 2613
Cdd:pfam12877  402 paATPSDGKQHRktnrpgNPMNGVseqlsSASIFEHVDRMsrgsadafrrssnkvqliamqpMPAPplhspplsdrsqes 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2614 ---KTKIQSALRHKSEIEHHRNKIRLRAKRRGHYEFPVVDDLSS--GDTKERHRVYRRAQMQIDKILDPAASVPSVFIEP 2688
Cdd:pfam12877  482 akiNKEIQKALRHKSEIEHHRNKIRLRAKRKGHYDFPAMDDIMKalTDRKEQRRIYQKAQKQIDKILDPDAHVPSPFTEP 561
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2689 RKSSRIKRSPKPRRKHQVNGCPADAEKDRLITTDSDGTYKRPPGVHNSAYIgcpSDPDLPADVQTPSSAELSRY------ 2762
Cdd:pfam12877  562 KKSSRGRRSPKQRRRQQNNGSPGDTEKDRLITRDSDGTYRKRPGVNNVAYV---SDPDQIPETNSPSPTDEVFYgpgsqp 638
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 537239411  2763 PGLPFSASQYIPPQPSIEEARQTMHSLLDDAFALVAPSS 2801
Cdd:pfam12877  639 KGHAPPPPPYLPPQPSIEEARQQMHSLLDDAFALVSPGS 677
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
868-977 6.23e-39

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 142.07  E-value: 6.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  868 LLFHATCRVHVDYICRNNFDWIINDSRETKYGKGNYFAKEAMYSHKNC---SYEAKNIVMLVARVLAGNSIEGNMRYSSA 944
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 537239411  945 PA--------LYDSCVDSRLNPSVFVIFQKEQIYPAYVIEY 977
Cdd:cd01439    81 PLkpsgveldRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
5-66 2.93e-32

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


Pssm-ID: 465819  Cd Length: 62  Bit Score: 120.97  E-value: 2.93e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537239411     5 GVCCFITKILCAHGGRMTLEELLAEIALPEAQLRELLEAAGPDRFVQLEIVGQTGVTRSVVA 66
Cdd:pfam18606    1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
822-977 1.61e-16

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 80.46  E-value: 1.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411   822 EYATISELFKASM----KYF-KIVSIKRIWNQDLWETFERKKlmmKNDNEMLLFHATCRVHVDYICRNNF--DWIINDSR 894
Cdd:pfam00644    3 EYQIIEKYFLSTHdpthGYPlFILEIFRVQRDGEWERFQPKK---KLRNRRLLWHGSRLTNFLGILSQGLriAPPEAPVT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411   895 ETKYGKGNYFAKEAMYSHKNC-SYEAKNI-VMLVARVLAGNSIE--GNMRYSSAPALYDSCV------------------ 952
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCpPSEAHGNgLMLLSEVALGDMNElkKADYAEKLPPGKHSVKglgktapesfvdldgvpl 159
                          170       180       190
                   ....*....|....*....|....*....|....
gi 537239411   953 ---------DSRLNPSVFVIFQKEQIYPAYVIEY 977
Cdd:pfam00644  160 gklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
143-170 7.83e-15

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


Pssm-ID: 436636  Cd Length: 28  Bit Score: 70.19  E-value: 7.83e-15
                           10        20
                   ....*....|....*....|....*...
gi 537239411   143 PFFMPEICKSYKGEGRKQICGQPQPCER 170
Cdd:pfam18633    1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
1776-2092 3.16e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 59.20  E-value: 3.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1776 DFSAPAPSRSdvlALPSLTSSDPSTFLSQLFPTMTETFSLSNSidlQSPQLFVLNPTSLEPSQPWSSSDLLMKTVTLLPS 1855
Cdd:pfam17823   96 DLSEPATREG---AADGAASRALAAAASSSPSSAAQSLPAAIA---ALPSEAFSAPRAAACRANASAAPRAAIAAASAPH 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1856 HSemSPLPSSPLDSlkldeawrvsliesdvhlTSAFSDTTCVFDFSLIPHDSSVSTLVP----SSSETSLGISTAGTPLS 1931
Cdd:pfam17823  170 AA--SPAPRTAASS------------------TTAASSTTAASSAPTTAASSAPATLTPargiSTAATATGHPAAGTALA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1932 SLPTVS-----------HLTP--ILTESSPFSTLTPSDSSVSMTD---------HHTPVSLMSSSVIPTS---TESVSDL 1986
Cdd:pfam17823  230 AVGNSSpaagtvtaavgTVTPaaLATLAAAAGTVASAAGTINMGDpharrlspaKHMPSDTMARNPAAPMgaqAQGPIIQ 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1987 YLSASPTLASEVSPSPMPTRPVMGSSLIPTDLPPSTSPEPSSSPEPSMPDISTAPGDTVDSALNSEPMSQNPQGNSVPPP 2066
Cdd:pfam17823  310 VSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPT 389
                          330       340
                   ....*....|....*....|....*...
gi 537239411  2067 QPSLGPEITSTLE--ATVGTPALATAKP 2092
Cdd:pfam17823  390 QGAAGPGILLAPEqvATEATAGTASAGP 417
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
689-757 3.33e-07

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 49.60  E-value: 3.33e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411   689 LWYWKDEFNKYVQYGDENkshlssnisSSYLESFFQS-CPRGVLPFQAGSQNYELSFQGMIQTNIASKTQ 757
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEV---------SSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTT 61
PHA03247 PHA03247
large tegument protein UL36; Provisional
2522-3043 1.52e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2522 PAPLPGPVKDHTTPSENgdvPSPKSKVPSKNIR-HRGRVSPSDADSTVSEESSERDAGDKAPATAhESKAHR---APQSG 2597
Cdd:PHA03247 2556 PPAAPPAAPDRSVPPPR---PAPRPSEPAVTSRaRRPDAPPQSARPRAPVDDRGDPRGPAPPSPL-PPDTHApdpPPPSP 2631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2598 LSLSFFPVLTVVMARPKTKIQSALRHKSEIEHHRnkirlRAKRRGHYEFPvvddlSSGDTKERHRVYRRAQMQIDKILDP 2677
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR-----RARRLGRAAQA-----SSPPQRPRRRAARPTVGSLTSLADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2678 AASVPSVfiEPRKSSRIKRSPKPRRKHQVNGCPADAEKDRLittdsdgtykrPPGVHNSAYIgcPSDPDLPADVQTPSSA 2757
Cdd:PHA03247 2702 PPPPPTP--EPAPHALVSATPLPPGPAAARQASPALPAAPA-----------PPAVPAGPAT--PGGPARPARPPTTAGP 2766
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2758 ELSRYPGLPFSASQYIPPQPSIEEARQTMHSLlddafalvaPS-SQPANALGTGPGVPASLPVNSTPSREERRATqwgsf 2836
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESL---------PSpWDPADPPAAVLAPAAALPPAASPAGPLPPPT----- 2832
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2837 ySPAQTANNPCSSRYEDY----GMTPPSGLLPSRPSFGPgllPASelVPSEPSQPQSSAEASFA-ARGIYSEEMPSVVRP 2911
Cdd:PHA03247 2833 -SAQPTAPPPPPGPPPPSlplgGSVAPGGDVRRRPPSRS---PAA--KPAAPARPPVRRLARPAvSRSTESFALPPDQPE 2906
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2912 RPvgGTTGSQIQHLTQVGIASRIGAQPVEIPPGRGSQYGGPgwpvygeeEAGRREAGKCNNVYYVFQTHMLGHQEYsSSP 2991
Cdd:PHA03247 2907 RP--PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP--------TTDPAGAGEPSGAVPQPWLGALVPGRV-AVP 2975
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 537239411 2992 LFQVPRTS-GREPSAPPGNlTHRGLQGPGLGYPTSSTE-DLQPGHSSASLIKAI 3043
Cdd:PHA03247 2976 RFRVPQPApSREAPASSTP-PLTGHSLSRVSSWASSLAlHEETDPPPVSLKQTL 3028
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
688-757 1.49e-03

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 39.63  E-value: 1.49e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537239411    688 WLWYWKDEFNKYVQYGDENkshlssnisSSYLESFFQS--CPRGVLPFqagSQNYELSFQGMIQTNIASKTQ 757
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRV---------SEDIEEAYAAgkKLCELSIC---GFPYTIDFNAMTQYNQATGTT 60
 
Name Accession Description Interval E-value
DUF3827 pfam12877
Domain of unknown function (DUF3827); This family contains the Swiss:Q9HCM3 protein which has ...
2188-2801 0e+00

Domain of unknown function (DUF3827); This family contains the Swiss:Q9HCM3 protein which has been found to be fused fused to BRAF gene in many cases of pilocytic astrocytomas. The fusion is due mainly to a tandem duplication of 2 Mb at 7q34. Although nothing is known about the function of Swiss:Q9HCM3 protein, the BRAF protein is a well characterized oncoprotein. It is a serine/threonine protein kinase which is implicated in MAP/ERK signalling, a critical pathway for the regulation of cell division, differentiation and secretion.


Pssm-ID: 463737  Cd Length: 677  Bit Score: 857.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2188 VPEPRFQVQTVLQFVPPSVDTGFCNFTQSVEKGLMTALFEV-RKHQGVYNLTVQIVNVTIGSSRVTPRRGPVNIIFAVKG 2266
Cdd:pfam12877    4 VPDYKFQVHTVLQFVPQHVDVRFCNFSQRIEKGLQMAFAEVeRRSLETTNFTVQILNITNALPEAQAQSQPVDITFAVRD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2267 THGFLNGSEVSDLLRNLTVVEFSFYLGYPVLQIAEPFQYPQLNLSQLLKSSWVRTVLLGVVERQLHNEVFPAEMERKLAQ 2346
Cdd:pfam12877   84 SRGYLNGSVVSNLLRQLSAVEFSFYLGFPVLQIAEPFHYPELNTSQLLRSSWVRTVLLGVDDQRVNERSFQALMERRLAL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2347 LLSEVPTRRRMWRRATvSAGNSVVQVVNVSRLEGDDNPVQLIYFVENQDGERLSAAQSSDLINKVDLQRAAIILGYRIQG 2426
Cdd:pfam12877  164 LLGESLGQGRRFKRAT-TVGNYSVQIVRVSRLPGPDNPAELTYFVEGPNGERLPATAAAKILNTVDVQRAAIILGYRVQG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2427 TIAQPVDRVKRPSPESQSGNLWVVVGVVIPVLVVTVIVVILYWKLCRTDKLDFQPDTVANIQQRQKLQIPSVKGFDFAKQ 2506
Cdd:pfam12877  243 VLAQPVEKVKNPPSETQPNNLWIIVGVVVPIAVVVIIIIILYWKLCRTDKLEFQPDTMSNIQQRQKLQAPSVKGFDFAKQ 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2507 HLGQHNKDDILIIHEPAPLPGPVKDhTTPSENGDVPSPKSKV---PSKNIRHRGRVSPSDADSTVSEESSERDAGDKAP- 2582
Cdd:pfam12877  323 HLGQHSKDDVPVIQEPAPLPLPVKD-ATPSENGEVPTPKSKTsskTSRGERRRGRISPSDGDSVGSDESSKRESGEESPr 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2583 --ATAHESKAHR------APQSGL-----SLSFFPVLTVV----------------------MARP-------------- 2613
Cdd:pfam12877  402 paATPSDGKQHRktnrpgNPMNGVseqlsSASIFEHVDRMsrgsadafrrssnkvqliamqpMPAPplhspplsdrsqes 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2614 ---KTKIQSALRHKSEIEHHRNKIRLRAKRRGHYEFPVVDDLSS--GDTKERHRVYRRAQMQIDKILDPAASVPSVFIEP 2688
Cdd:pfam12877  482 akiNKEIQKALRHKSEIEHHRNKIRLRAKRKGHYDFPAMDDIMKalTDRKEQRRIYQKAQKQIDKILDPDAHVPSPFTEP 561
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  2689 RKSSRIKRSPKPRRKHQVNGCPADAEKDRLITTDSDGTYKRPPGVHNSAYIgcpSDPDLPADVQTPSSAELSRY------ 2762
Cdd:pfam12877  562 KKSSRGRRSPKQRRRQQNNGSPGDTEKDRLITRDSDGTYRKRPGVNNVAYV---SDPDQIPETNSPSPTDEVFYgpgsqp 638
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 537239411  2763 PGLPFSASQYIPPQPSIEEARQTMHSLLDDAFALVAPSS 2801
Cdd:pfam12877  639 KGHAPPPPPYLPPQPSIEEARQQMHSLLDDAFALVSPGS 677
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
868-977 6.23e-39

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 142.07  E-value: 6.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  868 LLFHATCRVHVDYICRNNFDWIINDSRETKYGKGNYFAKEAMYSHKNC---SYEAKNIVMLVARVLAGNSIEGNMRYSSA 944
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSkksPKADGLKEMFLARVLTGDYTQGHPGYRRP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 537239411  945 PA--------LYDSCVDSRLNPSVFVIFQKEQIYPAYVIEY 977
Cdd:cd01439    81 PLkpsgveldRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
HTH_53 pfam18606
Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor ...
5-66 2.93e-32

Zap helix turn helix N-terminal domain; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. This domain is a helix turn helix domain found at the N-terminal region constituting the top cockpit layer of the protein.


Pssm-ID: 465819  Cd Length: 62  Bit Score: 120.97  E-value: 2.93e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537239411     5 GVCCFITKILCAHGGRMTLEELLAEIALPEAQLRELLEAAGPDRFVQLEIVGQTGVTRSVVA 66
Cdd:pfam18606    1 TVCSFLTKILCAHGGRMALEELLGEIELSEAQLCEVLEAAGPERFVLLETGGEAGVTRSVVA 62
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
822-977 1.61e-16

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 80.46  E-value: 1.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411   822 EYATISELFKASM----KYF-KIVSIKRIWNQDLWETFERKKlmmKNDNEMLLFHATCRVHVDYICRNNF--DWIINDSR 894
Cdd:pfam00644    3 EYQIIEKYFLSTHdpthGYPlFILEIFRVQRDGEWERFQPKK---KLRNRRLLWHGSRLTNFLGILSQGLriAPPEAPVT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411   895 ETKYGKGNYFAKEAMYSHKNC-SYEAKNI-VMLVARVLAGNSIE--GNMRYSSAPALYDSCV------------------ 952
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCpPSEAHGNgLMLLSEVALGDMNElkKADYAEKLPPGKHSVKglgktapesfvdldgvpl 159
                          170       180       190
                   ....*....|....*....|....*....|....
gi 537239411   953 ---------DSRLNPSVFVIFQKEQIYPAYVIEY 977
Cdd:pfam00644  160 gklvatgydSSVLLYNEYVVYNVNQVRPKYLLEV 193
zf-CCCH_8 pfam18633
Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) ...
143-170 7.83e-15

Zinc-finger antiviral protein (ZAP) zinc finger domain 3; Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. N-terminal domain of ZAP is the major functional domain which contains four zinc-finger motifs. This entry represents the third zinc finger type CCCH.


Pssm-ID: 436636  Cd Length: 28  Bit Score: 70.19  E-value: 7.83e-15
                           10        20
                   ....*....|....*....|....*...
gi 537239411   143 PFFMPEICKSYKGEGRKQICGQPQPCER 170
Cdd:pfam18633    1 PFFLPEICKNYKGEGRKQICSQQPPCER 28
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
1776-2092 3.16e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 59.20  E-value: 3.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1776 DFSAPAPSRSdvlALPSLTSSDPSTFLSQLFPTMTETFSLSNSidlQSPQLFVLNPTSLEPSQPWSSSDLLMKTVTLLPS 1855
Cdd:pfam17823   96 DLSEPATREG---AADGAASRALAAAASSSPSSAAQSLPAAIA---ALPSEAFSAPRAAACRANASAAPRAAIAAASAPH 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1856 HSemSPLPSSPLDSlkldeawrvsliesdvhlTSAFSDTTCVFDFSLIPHDSSVSTLVP----SSSETSLGISTAGTPLS 1931
Cdd:pfam17823  170 AA--SPAPRTAASS------------------TTAASSTTAASSAPTTAASSAPATLTPargiSTAATATGHPAAGTALA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1932 SLPTVS-----------HLTP--ILTESSPFSTLTPSDSSVSMTD---------HHTPVSLMSSSVIPTS---TESVSDL 1986
Cdd:pfam17823  230 AVGNSSpaagtvtaavgTVTPaaLATLAAAAGTVASAAGTINMGDpharrlspaKHMPSDTMARNPAAPMgaqAQGPIIQ 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  1987 YLSASPTLASEVSPSPMPTRPVMGSSLIPTDLPPSTSPEPSSSPEPSMPDISTAPGDTVDSALNSEPMSQNPQGNSVPPP 2066
Cdd:pfam17823  310 VSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPT 389
                          330       340
                   ....*....|....*....|....*...
gi 537239411  2067 QPSLGPEITSTLE--ATVGTPALATAKP 2092
Cdd:pfam17823  390 QGAAGPGILLAPEqvATEATAGTASAGP 417
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
689-757 3.33e-07

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 49.60  E-value: 3.33e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411   689 LWYWKDEFNKYVQYGDENkshlssnisSSYLESFFQS-CPRGVLPFQAGSQNYELSFQGMIQTNIASKTQ 757
Cdd:pfam02825    1 VWEWEDDNGGWHPYDPEV---------SSLIEEAYQKgKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTT 61
PHA03247 PHA03247
large tegument protein UL36; Provisional
2522-3043 1.52e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2522 PAPLPGPVKDHTTPSENgdvPSPKSKVPSKNIR-HRGRVSPSDADSTVSEESSERDAGDKAPATAhESKAHR---APQSG 2597
Cdd:PHA03247 2556 PPAAPPAAPDRSVPPPR---PAPRPSEPAVTSRaRRPDAPPQSARPRAPVDDRGDPRGPAPPSPL-PPDTHApdpPPPSP 2631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2598 LSLSFFPVLTVVMARPKTKIQSALRHKSEIEHHRnkirlRAKRRGHYEFPvvddlSSGDTKERHRVYRRAQMQIDKILDP 2677
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPR-----RARRLGRAAQA-----SSPPQRPRRRAARPTVGSLTSLADP 2701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2678 AASVPSVfiEPRKSSRIKRSPKPRRKHQVNGCPADAEKDRLittdsdgtykrPPGVHNSAYIgcPSDPDLPADVQTPSSA 2757
Cdd:PHA03247 2702 PPPPPTP--EPAPHALVSATPLPPGPAAARQASPALPAAPA-----------PPAVPAGPAT--PGGPARPARPPTTAGP 2766
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2758 ELSRYPGLPFSASQYIPPQPSIEEARQTMHSLlddafalvaPS-SQPANALGTGPGVPASLPVNSTPSREERRATqwgsf 2836
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESL---------PSpWDPADPPAAVLAPAAALPPAASPAGPLPPPT----- 2832
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2837 ySPAQTANNPCSSRYEDY----GMTPPSGLLPSRPSFGPgllPASelVPSEPSQPQSSAEASFA-ARGIYSEEMPSVVRP 2911
Cdd:PHA03247 2833 -SAQPTAPPPPPGPPPPSlplgGSVAPGGDVRRRPPSRS---PAA--KPAAPARPPVRRLARPAvSRSTESFALPPDQPE 2906
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411 2912 RPvgGTTGSQIQHLTQVGIASRIGAQPVEIPPGRGSQYGGPgwpvygeeEAGRREAGKCNNVYYVFQTHMLGHQEYsSSP 2991
Cdd:PHA03247 2907 RP--PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP--------TTDPAGAGEPSGAVPQPWLGALVPGRV-AVP 2975
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 537239411 2992 LFQVPRTS-GREPSAPPGNlTHRGLQGPGLGYPTSSTE-DLQPGHSSASLIKAI 3043
Cdd:PHA03247 2976 RFRVPQPApSREAPASSTP-PLTGHSLSRVSSWASSLAlHEETDPPPVSLKQTL 3028
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
813-977 2.70e-04

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 45.28  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  813 LVELDSQDVEYATISELFKASMK-------------YFKIVSIKRIWNQDLWE--TFERKKLMMKN---DNEMLLFHATc 874
Cdd:cd01438    18 LLDLAPDDKEYQSVEEEMQSTIRehrdggnaggifnRYNIIRIQKVVNKKLREryCHRQKEIAEENhnhHNERMLFHGS- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537239411  875 rVHVDYICRNNFDwiindSRET----KYGKGNYFA----KEAMY-----------SHKNCSYEAKNIVMLVARVLAGNSI 935
Cdd:cd01438    97 -PFINAIIHKGFD-----ERHAyiggMFGAGIYFAenssKSNQYvygigggtgcpTHKDRSCYVCHRQMLFCRVTLGKSF 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 537239411  936 E--GNMRYSSAPALYDSCVDsrlNPSV-------FVIFQKEQIYPAYVIEY 977
Cdd:cd01438   171 LqfSAMKMAHAPPGHHSVIG---RPSVnglayaeYVIYRGEQAYPEYLITY 218
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
688-757 1.49e-03

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 39.63  E-value: 1.49e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 537239411    688 WLWYWKDEFNKYVQYGDENkshlssnisSSYLESFFQS--CPRGVLPFqagSQNYELSFQGMIQTNIASKTQ 757
Cdd:smart00678    1 YVWEYEGRNGKWWPYDPRV---------SEDIEEAYAAgkKLCELSIC---GFPYTIDFNAMTQYNQATGTT 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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